ID   TF_RAT                  Reviewed;         295 AA.
AC   P42533;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 134.
DE   RecName: Full=Tissue factor;
DE            Short=TF;
DE   AltName: Full=Coagulation factor III;
DE   AltName: CD_antigen=CD142;
DE   Flags: Precursor;
GN   Name=F3; Synonyms=Cf3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley;
RX   PubMed=8950776;
RA   Taby O., Rosenfield C.L., Bogdanov V., Nemerson Y., Taubman M.B.;
RT   "Cloning of the rat tissue factor cDNA and promoter: identification of a
RT   serum-response region.";
RL   Thromb. Haemost. 76:697-702(1996).
CC   -!- FUNCTION: Initiates blood coagulation by forming a complex with
CC       circulating factor VII or VIIa. The [TF:VIIa] complex activates factors
CC       IX or X by specific limited proteolysis. TF plays a role in normal
CC       hemostasis by initiating the cell-surface assembly and propagation of
CC       the coagulation protease cascade.
CC   -!- SUBUNIT: Interacts with HSPE; the interaction, inhibited by heparin,
CC       promotes the generation of activated factor X and activates coagulation
CC       in the presence of activated factor VII. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P13726}; Single-
CC       pass type I membrane protein {ECO:0000250|UniProtKB:P13726}.
CC   -!- SIMILARITY: Belongs to the tissue factor family. {ECO:0000305}.
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DR   EMBL; U07619; AAA16966.1; -; mRNA.
DR   AlphaFoldDB; P42533; -.
DR   SMR; P42533; -.
DR   STRING; 10116.ENSRNOP00000015836; -.
DR   GlyGen; P42533; 6 sites.
DR   PaxDb; P42533; -.
DR   UCSC; RGD:2587; rat.
DR   RGD; 2587; F3.
DR   eggNOG; ENOG502RA1F; Eukaryota.
DR   InParanoid; P42533; -.
DR   PhylomeDB; P42533; -.
DR   Reactome; R-RNO-140834; Extrinsic Pathway of Fibrin Clot Formation.
DR   PRO; PR:P42533; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0009986; C:cell surface; IDA:RGD.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:1905286; C:serine-type peptidase complex; ISO:RGD.
DR   GO; GO:0004896; F:cytokine receptor activity; IBA:GO_Central.
DR   GO; GO:0005543; F:phospholipid binding; ISO:RGD.
DR   GO; GO:0002020; F:protease binding; IPI:RGD.
DR   GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
DR   GO; GO:0002541; P:activation of plasma proteins involved in acute inflammatory response; ISO:RGD.
DR   GO; GO:0007568; P:aging; IEP:RGD.
DR   GO; GO:0007596; P:blood coagulation; ISO:RGD.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:RGD.
DR   GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; IEP:RGD.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; ISO:RGD.
DR   GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:RGD.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR   GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:RGD.
DR   GO; GO:0010641; P:positive regulation of platelet-derived growth factor receptor signaling pathway; ISO:RGD.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:RGD.
DR   GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IDA:RGD.
DR   GO; GO:0016485; P:protein processing; ISO:RGD.
DR   GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR   GO; GO:0034405; P:response to fluid shear stress; IEP:RGD.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR   GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR   GO; GO:0009266; P:response to temperature stimulus; IEP:RGD.
DR   GO; GO:0009611; P:response to wounding; IEP:RGD.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR015373; Interferon/interleukin_rcp_dom.
DR   InterPro; IPR001187; Tissue_factor.
DR   InterPro; IPR030472; Tissue_Factor_CS.
DR   PANTHER; PTHR20859:SF22; PTHR20859:SF22; 1.
DR   Pfam; PF09294; Interfer-bind; 1.
DR   Pfam; PF01108; Tissue_fac; 1.
DR   PIRSF; PIRSF002498; Tissue_factor_3; 1.
DR   PRINTS; PR00346; TISSUEFACTOR.
DR   SUPFAM; SSF49265; SSF49265; 2.
DR   PROSITE; PS00621; TISSUE_FACTOR; 1.
PE   2: Evidence at transcript level;
KW   Blood coagulation; Disulfide bond; Glycoprotein; Hemostasis; Lipoprotein;
KW   Membrane; Palmitate; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000250"
FT   CHAIN           29..295
FT                   /note="Tissue factor"
FT                   /id="PRO_0000033641"
FT   TOPO_DOM        29..252
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        253..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        276..295
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOTIF           246..248
FT                   /note="WKS motif"
FT   LIPID           276
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        38
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        58
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        95
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        109
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        170
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        201
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        76..84
FT                   /evidence="ECO:0000250"
FT   DISULFID        219..242
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   295 AA;  33444 MW;  EE4C15B4E3628D48 CRC64;
     MAIPMRPRLL AALAPTFLGF LLLQVAVGAG TPPGKAFNLT WISTDFKTIL EWQPKPTNYT
     YTVQISDRSR NWKYKCTGTT DTECDLTDEI VKDVNWTYEA RVLSVPWRNS THGKETLFGT
     HGEEPPFTNA RKFLPYRDTK IGQPVIQKYE QGGTKLKVTV KDSFTLVRKN GTFLTLRQVF
     GNDLGYILTY RKDSSTGRKT NTTHTNEFLI DVEKGVSYCF FAQAVIFSRK TNHKSPESIT
     KCTEQWKSVL GETLIIVGAV VFLVTVFIIL LTISLCKRRK NRAGQKRKNT PSRLA